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SMARCA4 loss results in cancer cell–intrinsic defects in expression of innate immune and inflammatory genes. A and B, Immunoblots of parental and SMARCA4 KO H2122 ( A ) and <t>HCC44</t> ( B ) cell lysates stained using anti-SMARCA4 and β-actin antibodies. C and D, Expression of STING1 , IL1β , and IFNβ mRNA levels was evaluated in parental and SMARCA4 KO H2122 ( C ) and HCC44 ( D ) cells treated with control and 10 μg/mL 2′3′-cGAMP for 6 hours ( n = 3 biological replicates) by qRT-PCR. E and F, STING1 , IL1β , IFNβ , and IRF3-P mRNA expression levels were evaluated in parental and SMARCA4 KO H2122 ( E ) and HCC44 ( F ) cells treated with control and 5 μg/mL poly (dA:dT) overnight ( n = 3 biological replicates) by qRT-PCR. G, HCC44 IL1β secretion was evaluated by ELISA. H, Immunoblot analysis of STING1, IL1β, IFNβ, IRF3, and IRF3-P in parental and SMARCA4 KO H2122 cells treated with control and 5 μg/mL poly (dA:dT) for 6 or 18 hours. I, Immunoblot showing inducible expression of SMARCA4 in SMARCA4 -deficient human lung cancer cell line H322 by administration of doxycycline (DOX; 1 μg/mL) with GFP as control. J, mRNA expression of STING1 , IL1β , and IFNβ by qRT-PCR in H322 control and SMARCA4 reconstituted cell line treated with control and 5 μg/mL poly (dA:dT) overnight ( n = 3 biological replicates). Data points represent the mean ± SEM. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001; ns, not significant, two-sided unpaired t test. CON, control; Par, parental.

Hcc44, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 107 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 94 stars, based on 107 article reviews

hcc44 - by Bioz Stars, 2026-03

94/100 stars

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1) Product Images from "Mutation of SMARCA4 Induces Cancer Cell–Intrinsic Defects in the Enhancer Landscape and Resistance to Immunotherapy"

Article Title: Mutation of SMARCA4 Induces Cancer Cell–Intrinsic Defects in the Enhancer Landscape and Resistance to Immunotherapy

Journal: Cancer Research

doi: 10.1158/0008-5472.CAN-24-2054

Figure Legend Snippet: SMARCA4 loss results in cancer cell–intrinsic defects in expression of innate immune and inflammatory genes. A and B, Immunoblots of parental and SMARCA4 KO H2122 ( A ) and HCC44 ( B ) cell lysates stained using anti-SMARCA4 and β-actin antibodies. C and D, Expression of STING1 , IL1β , and IFNβ mRNA levels was evaluated in parental and SMARCA4 KO H2122 ( C ) and HCC44 ( D ) cells treated with control and 10 μg/mL 2′3′-cGAMP for 6 hours ( n = 3 biological replicates) by qRT-PCR. E and F, STING1 , IL1β , IFNβ , and IRF3-P mRNA expression levels were evaluated in parental and SMARCA4 KO H2122 ( E ) and HCC44 ( F ) cells treated with control and 5 μg/mL poly (dA:dT) overnight ( n = 3 biological replicates) by qRT-PCR. G, HCC44 IL1β secretion was evaluated by ELISA. H, Immunoblot analysis of STING1, IL1β, IFNβ, IRF3, and IRF3-P in parental and SMARCA4 KO H2122 cells treated with control and 5 μg/mL poly (dA:dT) for 6 or 18 hours. I, Immunoblot showing inducible expression of SMARCA4 in SMARCA4 -deficient human lung cancer cell line H322 by administration of doxycycline (DOX; 1 μg/mL) with GFP as control. J, mRNA expression of STING1 , IL1β , and IFNβ by qRT-PCR in H322 control and SMARCA4 reconstituted cell line treated with control and 5 μg/mL poly (dA:dT) overnight ( n = 3 biological replicates). Data points represent the mean ± SEM. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001; ns, not significant, two-sided unpaired t test. CON, control; Par, parental.

Techniques Used: Expressing, Western Blot, Staining, Control, Quantitative RT-PCR, Enzyme-linked Immunosorbent Assay

SMARCA4 degradation abrogates cancer cell–intrinsic expression of innate immune and inflammatory genes. A, SMARCA4 WT cells (HCC44, H1792, and H1975) and SMARCA4 mutation cells (H322, H1693, and H1299) were treated with DMSO control or 1 μmol/L ACBI1 for 96 hours. Immunoblots of SMARCA4 and β-actin in SMARCA4 WT cells (left) and SMARCA4 mutation cells (right). B–D, RNA-seq analysis of SMARCA4 WT (HCC44, H1792, and H1975) cells treated with DMSO vs. 1 μmol/L ACBI1 for 96 hours. B, GSEA curves showing upregulation of the inflammatory response and TNFα_signaling_via_NF-κB pathway in DMSO treatment. NES, normalized enrichment score. C, GSEA of hallmark top enriched pathways in DMSO treatment. Inflammatory response and IFNα response are at the top positions. D, Heatmap presenting the top 50 upregulated and downregulated genes in DMSO treatment, with IL1β being the one of significantly upregulated genes. E, qRT-PCR analysis of IL1β expression from SMARCA4 WT cells (HCC44, H1792, and H1975) treated with DMSO vs. 1 μmol/L ACBI1 for 96 hours and SMARCA4 WT cells (HCC44, H1792, and H1975) vs. SMARCA4 mutation cells (H322, H1693, and H1299). F, STING1 mRNA expression from SMARCA4 WT cells (HCC44, H1792, and H1975) treated with DMSO vs. 1 μmol/L ACBI1 for 96 hours. G, Immunoblots of STING1 and VINCULIN in H1792 cells treated with 0.1 or 1 μmol/L ACBI1 for 96 hours. Data points represent the mean ± SEM. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001, two-sided unpaired t test. MUT, mutant.

Figure Legend Snippet: SMARCA4 degradation abrogates cancer cell–intrinsic expression of innate immune and inflammatory genes. A, SMARCA4 WT cells (HCC44, H1792, and H1975) and SMARCA4 mutation cells (H322, H1693, and H1299) were treated with DMSO control or 1 μmol/L ACBI1 for 96 hours. Immunoblots of SMARCA4 and β-actin in SMARCA4 WT cells (left) and SMARCA4 mutation cells (right). B–D, RNA-seq analysis of SMARCA4 WT (HCC44, H1792, and H1975) cells treated with DMSO vs. 1 μmol/L ACBI1 for 96 hours. B, GSEA curves showing upregulation of the inflammatory response and TNFα_signaling_via_NF-κB pathway in DMSO treatment. NES, normalized enrichment score. C, GSEA of hallmark top enriched pathways in DMSO treatment. Inflammatory response and IFNα response are at the top positions. D, Heatmap presenting the top 50 upregulated and downregulated genes in DMSO treatment, with IL1β being the one of significantly upregulated genes. E, qRT-PCR analysis of IL1β expression from SMARCA4 WT cells (HCC44, H1792, and H1975) treated with DMSO vs. 1 μmol/L ACBI1 for 96 hours and SMARCA4 WT cells (HCC44, H1792, and H1975) vs. SMARCA4 mutation cells (H322, H1693, and H1299). F, STING1 mRNA expression from SMARCA4 WT cells (HCC44, H1792, and H1975) treated with DMSO vs. 1 μmol/L ACBI1 for 96 hours. G, Immunoblots of STING1 and VINCULIN in H1792 cells treated with 0.1 or 1 μmol/L ACBI1 for 96 hours. Data points represent the mean ± SEM. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001, two-sided unpaired t test. MUT, mutant.

Techniques Used: Expressing, Mutagenesis, Control, Western Blot, RNA Sequencing, Quantitative RT-PCR

Loss of SMARCA4 abrogates chromatin accessibility at enhancers associated with innate immune inflammation and are co-occupied by NF-κB. SMARCA4 WT cells (HCC44 and H1792) were treated with DMSO control or 1 μmol/L ACBI1 for 96 hours. A, Venn diagrams illustrating alterations in chromatin accessibility upon ACBI1 treatment along with annotation of ATAC peaks distribution across the genomic regions. B, ATAC-seq read density heatmaps for total peaks with DMSO and ACBI1 treatment in HCC44 and H1975. C, ATAC-seq read density heatmaps for enhancer peaks with DMSO and ACBI1 treatment in HCC44 and H1975. D, Pathway enrichment analysis for lost peaks in HCC44 and H1975 with ACBI1 treatment. E, Examination of transcription factor motifs on enhancers with lost accessibility with ACBI1 treatment as identified in D . F, Genome browser tracks of chromatin accessibility at IFNβ loci ( n = 2 biological replicates) in H1975 cells, following with representative integrative genome viewer tracks of views of the SMARCA4 and NF-κB CUT&RUN peaks on the IFNβ genomic locus. H3K27ac peaks derived from ChIP-seq denote putative enhancers. The overlapping peaks with differential intensity in the ACBI1 treatment group are highlighted. G, Endogenous interactions of SMARCA4 and NF-κB were analyzed by coimmunoprecipitation.

Figure Legend Snippet: Loss of SMARCA4 abrogates chromatin accessibility at enhancers associated with innate immune inflammation and are co-occupied by NF-κB. SMARCA4 WT cells (HCC44 and H1792) were treated with DMSO control or 1 μmol/L ACBI1 for 96 hours. A, Venn diagrams illustrating alterations in chromatin accessibility upon ACBI1 treatment along with annotation of ATAC peaks distribution across the genomic regions. B, ATAC-seq read density heatmaps for total peaks with DMSO and ACBI1 treatment in HCC44 and H1975. C, ATAC-seq read density heatmaps for enhancer peaks with DMSO and ACBI1 treatment in HCC44 and H1975. D, Pathway enrichment analysis for lost peaks in HCC44 and H1975 with ACBI1 treatment. E, Examination of transcription factor motifs on enhancers with lost accessibility with ACBI1 treatment as identified in D . F, Genome browser tracks of chromatin accessibility at IFNβ loci ( n = 2 biological replicates) in H1975 cells, following with representative integrative genome viewer tracks of views of the SMARCA4 and NF-κB CUT&RUN peaks on the IFNβ genomic locus. H3K27ac peaks derived from ChIP-seq denote putative enhancers. The overlapping peaks with differential intensity in the ACBI1 treatment group are highlighted. G, Endogenous interactions of SMARCA4 and NF-κB were analyzed by coimmunoprecipitation.

Techniques Used: Control, Derivative Assay, ChIP-sequencing

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Journal: Cancer Research

Article Title: Mutation of SMARCA4 Induces Cancer Cell–Intrinsic Defects in the Enhancer Landscape and Resistance to Immunotherapy

doi: 10.1158/0008-5472.CAN-24-2054

Figure Lengend Snippet: SMARCA4 loss results in cancer cell–intrinsic defects in expression of innate immune and inflammatory genes. A and B, Immunoblots of parental and SMARCA4 KO H2122 ( A ) and HCC44 ( B ) cell lysates stained using anti-SMARCA4 and β-actin antibodies. C and D, Expression of STING1 , IL1β , and IFNβ mRNA levels was evaluated in parental and SMARCA4 KO H2122 ( C ) and HCC44 ( D ) cells treated with control and 10 μg/mL 2′3′-cGAMP for 6 hours ( n = 3 biological replicates) by qRT-PCR. E and F, STING1 , IL1β , IFNβ , and IRF3-P mRNA expression levels were evaluated in parental and SMARCA4 KO H2122 ( E ) and HCC44 ( F ) cells treated with control and 5 μg/mL poly (dA:dT) overnight ( n = 3 biological replicates) by qRT-PCR. G, HCC44 IL1β secretion was evaluated by ELISA. H, Immunoblot analysis of STING1, IL1β, IFNβ, IRF3, and IRF3-P in parental and SMARCA4 KO H2122 cells treated with control and 5 μg/mL poly (dA:dT) for 6 or 18 hours. I, Immunoblot showing inducible expression of SMARCA4 in SMARCA4 -deficient human lung cancer cell line H322 by administration of doxycycline (DOX; 1 μg/mL) with GFP as control. J, mRNA expression of STING1 , IL1β , and IFNβ by qRT-PCR in H322 control and SMARCA4 reconstituted cell line treated with control and 5 μg/mL poly (dA:dT) overnight ( n = 3 biological replicates). Data points represent the mean ± SEM. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001; ns, not significant, two-sided unpaired t test. CON, control; Par, parental.

Article Snippet: H2122 (RRID: CVCL_1531), HCC44 (RRID: CVCL_2060), H1792 (RRID: CVCL_1495), H1975 (RRID: CVCL_1511), H1693 (RRID: CVCL_1488), H1299 (RRID: CVCL_0060), and H322 were purchased from the ATCC.

Techniques: Expressing, Western Blot, Staining, Control, Quantitative RT-PCR, Enzyme-linked Immunosorbent Assay

Journal: Cancer Research

Article Title: Mutation of SMARCA4 Induces Cancer Cell–Intrinsic Defects in the Enhancer Landscape and Resistance to Immunotherapy

doi: 10.1158/0008-5472.CAN-24-2054

Figure Lengend Snippet: SMARCA4 degradation abrogates cancer cell–intrinsic expression of innate immune and inflammatory genes. A, SMARCA4 WT cells (HCC44, H1792, and H1975) and SMARCA4 mutation cells (H322, H1693, and H1299) were treated with DMSO control or 1 μmol/L ACBI1 for 96 hours. Immunoblots of SMARCA4 and β-actin in SMARCA4 WT cells (left) and SMARCA4 mutation cells (right). B–D, RNA-seq analysis of SMARCA4 WT (HCC44, H1792, and H1975) cells treated with DMSO vs. 1 μmol/L ACBI1 for 96 hours. B, GSEA curves showing upregulation of the inflammatory response and TNFα_signaling_via_NF-κB pathway in DMSO treatment. NES, normalized enrichment score. C, GSEA of hallmark top enriched pathways in DMSO treatment. Inflammatory response and IFNα response are at the top positions. D, Heatmap presenting the top 50 upregulated and downregulated genes in DMSO treatment, with IL1β being the one of significantly upregulated genes. E, qRT-PCR analysis of IL1β expression from SMARCA4 WT cells (HCC44, H1792, and H1975) treated with DMSO vs. 1 μmol/L ACBI1 for 96 hours and SMARCA4 WT cells (HCC44, H1792, and H1975) vs. SMARCA4 mutation cells (H322, H1693, and H1299). F, STING1 mRNA expression from SMARCA4 WT cells (HCC44, H1792, and H1975) treated with DMSO vs. 1 μmol/L ACBI1 for 96 hours. G, Immunoblots of STING1 and VINCULIN in H1792 cells treated with 0.1 or 1 μmol/L ACBI1 for 96 hours. Data points represent the mean ± SEM. *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001, two-sided unpaired t test. MUT, mutant.

Techniques: Expressing, Mutagenesis, Control, Western Blot, RNA Sequencing, Quantitative RT-PCR

Journal: Cancer Research

Article Title: Mutation of SMARCA4 Induces Cancer Cell–Intrinsic Defects in the Enhancer Landscape and Resistance to Immunotherapy

doi: 10.1158/0008-5472.CAN-24-2054

Figure Lengend Snippet: Loss of SMARCA4 abrogates chromatin accessibility at enhancers associated with innate immune inflammation and are co-occupied by NF-κB. SMARCA4 WT cells (HCC44 and H1792) were treated with DMSO control or 1 μmol/L ACBI1 for 96 hours. A, Venn diagrams illustrating alterations in chromatin accessibility upon ACBI1 treatment along with annotation of ATAC peaks distribution across the genomic regions. B, ATAC-seq read density heatmaps for total peaks with DMSO and ACBI1 treatment in HCC44 and H1975. C, ATAC-seq read density heatmaps for enhancer peaks with DMSO and ACBI1 treatment in HCC44 and H1975. D, Pathway enrichment analysis for lost peaks in HCC44 and H1975 with ACBI1 treatment. E, Examination of transcription factor motifs on enhancers with lost accessibility with ACBI1 treatment as identified in D . F, Genome browser tracks of chromatin accessibility at IFNβ loci ( n = 2 biological replicates) in H1975 cells, following with representative integrative genome viewer tracks of views of the SMARCA4 and NF-κB CUT&RUN peaks on the IFNβ genomic locus. H3K27ac peaks derived from ChIP-seq denote putative enhancers. The overlapping peaks with differential intensity in the ACBI1 treatment group are highlighted. G, Endogenous interactions of SMARCA4 and NF-κB were analyzed by coimmunoprecipitation.

Techniques: Control, Derivative Assay, ChIP-sequencing

Journal: Journal of cellular biochemistry

Article Title: Pediatric Brain Tumor Cell Lines

doi: 10.1002/jcb.24976

Figure Lengend Snippet: Pediatric Brain Tumors, Summary

Article Snippet: PFSK-1 , PNET , 22 mo , M , 1992 , ATCC , Y , N , ** , [ 53 ];CRL-2060.

Techniques:

Current available pediatric brain tumor cell lines in literature.

Journal: Journal of cellular biochemistry

Article Title: Pediatric Brain Tumor Cell Lines

doi: 10.1002/jcb.24976

Figure Lengend Snippet: Current available pediatric brain tumor cell lines in literature.

Article Snippet: PFSK-1 , PNET , 22 mo , M , 1992 , ATCC , Y , N , ** , [ 53 ];CRL-2060.

Techniques: Biomarker Discovery, In Vivo

(a) Natalizumab binding on VLA-4 expressing cells (PFSK1) compared with non-expressing cells (HEK293/T17) by flow cytometry using an FITC-conjugated secondary anti-IgG 4 . (b) Effect of natalizumab blocking antibody HCA250 on natalizumab and milk (T2) IgG 4 binding to PFSK1 cells. Serum was used at 1:40 dilution. Each column corresponds to average binding of IgG 4 on PFSK1 (geometric mean of the florescence intensity – GMFI – of cells incubated with the sample) from three replicates. Error bars are standard error. (c) Stability of expression of VLA-4 by PFSK1 cells. PFSK1 cells from passages 7 to 13 were incubated with either natalizumab at 10 µg/ml or with secondary only control. p -value for comparing binding of natalizumab to secondary only was calculated using unpaired t -test. Variances were compared using F -test. (d) Natalizumab detection in serum from treated patients positive for anti-natalizumab antibodies were compared with anti-natalizumab negative samples ( p < 0.0001, Mann–Whitney test) using an anti-IgG 4 antibody. Each dot corresponds to the binding of IgG 4 on PFSK1 (ratio of GMFI of cells incubated with the sample to cells incubated only with secondary antibody) from each serum sample, tested in three independent experiments.

Journal: Therapeutic Advances in Neurological Disorders

Article Title: Natalizumab in cerebrospinal fluid and breastmilk of patients with multiple sclerosis

doi: 10.1177/17562864221150040

Figure Lengend Snippet: (a) Natalizumab binding on VLA-4 expressing cells (PFSK1) compared with non-expressing cells (HEK293/T17) by flow cytometry using an FITC-conjugated secondary anti-IgG 4 . (b) Effect of natalizumab blocking antibody HCA250 on natalizumab and milk (T2) IgG 4 binding to PFSK1 cells. Serum was used at 1:40 dilution. Each column corresponds to average binding of IgG 4 on PFSK1 (geometric mean of the florescence intensity – GMFI – of cells incubated with the sample) from three replicates. Error bars are standard error. (c) Stability of expression of VLA-4 by PFSK1 cells. PFSK1 cells from passages 7 to 13 were incubated with either natalizumab at 10 µg/ml or with secondary only control. p -value for comparing binding of natalizumab to secondary only was calculated using unpaired t -test. Variances were compared using F -test. (d) Natalizumab detection in serum from treated patients positive for anti-natalizumab antibodies were compared with anti-natalizumab negative samples ( p < 0.0001, Mann–Whitney test) using an anti-IgG 4 antibody. Each dot corresponds to the binding of IgG 4 on PFSK1 (ratio of GMFI of cells incubated with the sample to cells incubated only with secondary antibody) from each serum sample, tested in three independent experiments.

Article Snippet: PFSK1 cells and HEK293 cells were purchased from ATCC (LGC, Wesel, Germany; CRL-2060 and CRL-11268, respectively).

Techniques: Binding Assay, Expressing, Flow Cytometry, Blocking Assay, Incubation, Control, MANN-WHITNEY

(a) IgG binding on PFSK1 cells from CSF of MS donors compared with non-inflammatory controls ( p = 0.008, Mann–Whitney test) using an anti-IgG antibody. Each dot corresponds to the binding of IgG on PFSK1 (ratio of geometric mean of the florescence intensity – GMFI – of cells incubated with the sample to cells incubated only with secondary antibody) from each CSF sample. (b) IgG binding on PFSK1 cells in natalizumab treated compared with untreated patients; results from two independently tested cohorts are pooled and expressed as the number of standard deviations by which each sample is above or below the mean value of the control samples ( p < 0.0001, Mann–Whitney test). Each dot corresponds to one sample. (c) Natalizumab detection in CSF from treated patients compared with untreated patients ( p < 0.0015, Mann–Whitney test) using an anti-IgG 4 antibody. Each dot corresponds to the binding of IgG 4 on PFSK1 (ratio of geometric mean of the florescence intensity – GMFI – of cells incubated with the sample to cells incubated only with secondary antibody) from each serum sample. (d) Natalizumab detection in serum from treated patients compared with untreated patients ( p < 0.0018, Mann–Whitney test) using an anti-IgG 4 antibody. Each dot corresponds to the binding of IgG 4 on PFSK1 (ratio of GMFI of cells incubated with the sample to cells incubated only with secondary antibody) from each serum sample.

Journal: Therapeutic Advances in Neurological Disorders

Article Title: Natalizumab in cerebrospinal fluid and breastmilk of patients with multiple sclerosis

doi: 10.1177/17562864221150040

Figure Lengend Snippet: (a) IgG binding on PFSK1 cells from CSF of MS donors compared with non-inflammatory controls ( p = 0.008, Mann–Whitney test) using an anti-IgG antibody. Each dot corresponds to the binding of IgG on PFSK1 (ratio of geometric mean of the florescence intensity – GMFI – of cells incubated with the sample to cells incubated only with secondary antibody) from each CSF sample. (b) IgG binding on PFSK1 cells in natalizumab treated compared with untreated patients; results from two independently tested cohorts are pooled and expressed as the number of standard deviations by which each sample is above or below the mean value of the control samples ( p < 0.0001, Mann–Whitney test). Each dot corresponds to one sample. (c) Natalizumab detection in CSF from treated patients compared with untreated patients ( p < 0.0015, Mann–Whitney test) using an anti-IgG 4 antibody. Each dot corresponds to the binding of IgG 4 on PFSK1 (ratio of geometric mean of the florescence intensity – GMFI – of cells incubated with the sample to cells incubated only with secondary antibody) from each serum sample. (d) Natalizumab detection in serum from treated patients compared with untreated patients ( p < 0.0018, Mann–Whitney test) using an anti-IgG 4 antibody. Each dot corresponds to the binding of IgG 4 on PFSK1 (ratio of GMFI of cells incubated with the sample to cells incubated only with secondary antibody) from each serum sample.

Article Snippet: PFSK1 cells and HEK293 cells were purchased from ATCC (LGC, Wesel, Germany; CRL-2060 and CRL-11268, respectively).

Techniques: Binding Assay, MANN-WHITNEY, Incubation, Control

Journal: Therapeutic Advances in Neurological Disorders

Article Title: Natalizumab in cerebrospinal fluid and breastmilk of patients with multiple sclerosis

doi: 10.1177/17562864221150040

Article Snippet: PFSK1 cells and HEK293 cells were purchased from ATCC (LGC, Wesel, Germany; CRL-2060 and CRL-11268, respectively).

Techniques: Binding Assay, Expressing, Flow Cytometry, Blocking Assay, Incubation, Control, MANN-WHITNEY

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